1d6y

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[[Image:1d6y.jpg|left|200px]]
[[Image:1d6y.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1d6y |SIZE=350|CAPTION= <scene name='initialview01'>1d6y</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1d6y", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HY1:PHENYLACETALDEHYDE'>HY1</scene>, <scene name='pdbligand=NO:NITROGEN+OXIDE'>NO</scene>, <scene name='pdbligand=PEA:2-PHENYLETHYLAMINE'>PEA</scene>, <scene name='pdbligand=TYQ:3-AMINO-6-HYDROXY-TYROSINE'>TYQ</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1d6y| PDB=1d6y | SCENE= }}
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|RELATEDENTRY=[[1oac|1OAC]], [[1spu|1SPU]], [[1jez|1JEZ]], [[1qaf|1QAF]], [[1qak|1QAK]], [[1qal|1QAL]], [[1d6u|1D6U]], [[1d6y|1D6Y]], [[1d6z|1D6Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d6y OCA], [http://www.ebi.ac.uk/pdbsum/1d6y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d6y RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.'''
'''CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.'''
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==Reference==
==Reference==
Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10576737 10576737]
Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10576737 10576737]
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[[Category: Amine oxidase (copper-containing)]]
 
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Phillips, S E.V.]]
[[Category: Phillips, S E.V.]]
[[Category: Wilmot, C M.]]
[[Category: Wilmot, C M.]]
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[[Category: reaction intermediate mimic]]
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[[Category: Reaction intermediate mimic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:31:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:35:53 2008''
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Revision as of 10:31, 2 May 2008

Image:1d6y.jpg

Template:STRUCTURE 1d6y

CRYSTAL STRUCTURE OF E. COLI COPPER-CONTAINING AMINE OXIDASE ANAEROBICALLY REDUCED WITH BETA-PHENYLETHYLAMINE AND COMPLEXED WITH NITRIC OXIDE.


Overview

X-ray crystal structures of three species related to the oxidative half of the reaction of the copper-containing quinoprotein amine oxidase from Escherichia coli have been determined. Crystals were freeze-trapped either anaerobically or aerobically after exposure to substrate, and structures were determined to resolutions between 2.1 and 2.4 angstroms. The oxidation state of the quinone cofactor was investigated by single-crystal spectrophotometry. The structures reveal the site of bound dioxygen and the proton transfer pathways involved in oxygen reduction. The quinone cofactor is regenerated from the iminoquinone intermediate by hydrolysis involving Asp383, the catalytic base in the reductive half-reaction. Product aldehyde inhibits the hydrolysis, making release of product the rate-determining step of the reaction in the crystal.

About this Structure

1D6Y is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Visualization of dioxygen bound to copper during enzyme catalysis., Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE, Science. 1999 Nov 26;286(5445):1724-8. PMID:10576737 Page seeded by OCA on Fri May 2 13:31:16 2008

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